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- Title
Inactivation of the three GGA genes in HeLa cells partially compromises lysosomal enzyme sorting.
- Authors
Doray, Balraj; Liu, Lin; Lee, Wang‐Sik; Jennings, Benjamin C.; Kornfeld, Stuart
- Abstract
The Golgi‐localized, gamma‐ear containing, ADP‐ribosylation factor‐binding proteins (GGAs 1, 2, and 3) are multidomain proteins that bind mannose 6‐phosphate receptors (MPRs) at the Golgi and play a role, along with adaptor protein complex 1 (AP‐1), in the sorting of newly synthesized lysosomal hydrolases to the endolysosomal system. However, the relative importance of the two types of coat proteins in this process is still unclear. Here, we report that inactivation of all three GGA genes in HeLa cells decreased the sorting efficiency of cathepsin D from 97% to 73% relative to wild‐type, with marked redistribution of the cation‐independent MPR from peripheral punctae to the trans‐Golgi network. In comparison, GNPTAB−/− HeLa cells with complete inactivation of the mannose 6‐phosphate pathway sorted only 20% of the cathepsin D. We conclude that the residual sorting of cathepsin D in the GGA triple‐knockout cells is mediated by AP‐1.
- Subjects
GENES; CATHEPSIN D; ENZYMES; HYDROLASES; ADP-ribosylation; MYELOID differentiation factor 88; ADAPTOR proteins; LYSOSOMES
- Publication
FEBS Open Bio, 2021, Vol 11, Issue 2, p367
- ISSN
2211-5463
- Publication type
Article
- DOI
10.1002/2211-5463.13040